TY - JOUR
T1 - NetSurfP-3.0
T2 - accurate and fast prediction of protein structural features by protein language models and deep learning
AU - Høie, Magnus Haraldson
AU - Kiehl, Erik Nicolas
AU - Petersen, Bent
AU - Nielsen, Morten
AU - Winther, Ole
AU - Nielsen, Henrik
AU - Hallgren, Jeppe
AU - Marcatili, Paolo
N1 - © The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.
PY - 2022/7/5
Y1 - 2022/7/5
N2 - Recent advances in machine learning and natural language processing have made it possible to profoundly advance our ability to accurately predict protein structures and their functions. While such improvements are significantly impacting the fields of biology and biotechnology at large, such methods have the downside of high demands in terms of computing power and runtime, hampering their applicability to large datasets. Here, we present NetSurfP-3.0, a tool for predicting solvent accessibility, secondary structure, structural disorder and backbone dihedral angles for each residue of an amino acid sequence. This NetSurfP update exploits recent advances in pre-trained protein language models to drastically improve the runtime of its predecessor by two orders of magnitude, while displaying similar prediction performance. We assessed the accuracy of NetSurfP-3.0 on several independent test datasets and found it to consistently produce state-of-the-art predictions for each of its output features, with a runtime that is up to to 600 times faster than the most commonly available methods performing the same tasks. The tool is freely available as a web server with a user-friendly interface to navigate the results, as well as a standalone downloadable package.
AB - Recent advances in machine learning and natural language processing have made it possible to profoundly advance our ability to accurately predict protein structures and their functions. While such improvements are significantly impacting the fields of biology and biotechnology at large, such methods have the downside of high demands in terms of computing power and runtime, hampering their applicability to large datasets. Here, we present NetSurfP-3.0, a tool for predicting solvent accessibility, secondary structure, structural disorder and backbone dihedral angles for each residue of an amino acid sequence. This NetSurfP update exploits recent advances in pre-trained protein language models to drastically improve the runtime of its predecessor by two orders of magnitude, while displaying similar prediction performance. We assessed the accuracy of NetSurfP-3.0 on several independent test datasets and found it to consistently produce state-of-the-art predictions for each of its output features, with a runtime that is up to to 600 times faster than the most commonly available methods performing the same tasks. The tool is freely available as a web server with a user-friendly interface to navigate the results, as well as a standalone downloadable package.
UR - http://www.scopus.com/inward/record.url?scp=85134367245&partnerID=8YFLogxK
U2 - 10.1093/nar/gkac439
DO - 10.1093/nar/gkac439
M3 - Journal article
C2 - 35648435
SN - 0305-1048
VL - 50
SP - W510-W515
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - W1
ER -